Journal article

Synthesis, conformational studies and biological activity of N-alpha-mono-biotinylated rat relaxin

MN Mathieu, JD Wade, B Catimel, CP Bond, EC Nice, RJ Summers, L Otvos, GW Tregear

JOURNAL OF PEPTIDE RESEARCH | MUNKSGAARD INT PUBL LTD | Published : 2001

Abstract

Biotin-avidin immobilization can be a useful tool in structure-function studies of hormone receptors. A crucial step is the preparation of a specifically biotinylated hormone that is able to bind to its receptor while leaving the biotin group free for interaction with avidin. The receptor for relaxin, an ovarian peptidic hormone produced during pregnancy, has not yet been isolated. We therefore undertook to prepare a specifically monobiotinylated rat relaxin for use in ligand-searching strategies. Rat relaxin is a convenient analogue because reliable bioassays exist, thus allowing assessment of the effect of N-biotinylation on bioactivity. To help improve the yield of the two-chain, three-di..

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